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Database: UniProt
Entry: A0A1V8T2A9_9PEZI
LinkDB: A0A1V8T2A9_9PEZI
Original site: A0A1V8T2A9_9PEZI 
ID   A0A1V8T2A9_9PEZI        Unreviewed;       508 AA.
AC   A0A1V8T2A9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|RuleBase:RU365074};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN   ORFNames=B0A48_09326 {ECO:0000313|EMBL:OQO05556.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO05556.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the N(1) position of adenine in helix 25.1 in
CC       25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis.
CC       Required for efficient pre-rRNA cleavage at site A2.
CC       {ECO:0000256|RuleBase:RU365074}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU365074}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC       {ECO:0000256|ARBA:ARBA00006301, ECO:0000256|RuleBase:RU365074}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQO05556.1}.
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DR   EMBL; NAJO01000019; OQO05556.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8T2A9; -.
DR   STRING; 1507870.A0A1V8T2A9; -.
DR   InParanoid; A0A1V8T2A9; -.
DR   OrthoDB; 1694at2759; -.
DR   Proteomes; UP000192596; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.2150; Ribosomal RNA-processing protein 8, N-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR007823; RRP8.
DR   InterPro; IPR042036; RRP8_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12787:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 1.
DR   PANTHER; PTHR12787; UNCHARACTERIZED; 1.
DR   Pfam; PF05148; Methyltransf_8; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU365074};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW   ECO:0000256|RuleBase:RU365074};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU365074};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365074}.
FT   REGION          29..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..155
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  55572 MW;  3B1FDFFECF53FD19 CRC64;
     MFAVKGWKVD PSTLTKQTEV FKSAKALEKA EDKADKTRKR KRRQDAGTVS EVDLGKQWER
     HVEGKKGTGA NSGTVGVRER KKQKKEPAAE TETGKVAEET VGDVATEDVE ATVPAKDKKS
     KKKRKPSTPS NDAAAAAPPA TGPKAQPPPP TPTVASANLT PMQSAMRQKL ISARFRHLNQ
     TLYTAPSAEA SALFTTDPKM FEDYHAGFRQ QVDVWPENPV DSFISTIRQR AKIPQPSRAA
     KAKGKDGLDA GLTHLPTTKG TCIIADLGCG DARLARTLTT SNETSSLNLK LHSFDLHSPS
     KYVVKADISS LPLEGDSVDV AIFCLALMGT NWISFIEEAY RILHWKGELW VAEIKSRFGR
     VGKKGKVVEH SVGSKRKAAA LAKVKESRKK EADGANEDAV LRMEVDGVEP AVQQETDVSA
     FVEVLKKRGF VLREGEGSVD LGNKMFVKME FIKAAAPSKG KGAKSEEASG KERRPMHAQK
     KFLDQQKDEE ITTEDEAKVL KPCLYKIR
//
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